ID   A0A091FFQ8_9AVES        Unreviewed;      1075 AA.
AC   A0A091FFQ8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000256|ARBA:ARBA00040077};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=N303_12960 {ECO:0000313|EMBL:KFO69460.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO69460.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO69460.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO69460.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ubiquitin-protein ligase that probably functions as an E3
CC       ligase in conjunction with specific E1 and E2 ligases. May also
CC       function as an E4 ligase mediating the assembly of polyubiquitin chains
CC       on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates
CC       'Lys-48'-linked polyubiquitination of substrates.
CC       {ECO:0000256|ARBA:ARBA00037624}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000256|ARBA:ARBA00007434}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL447068; KFO69460.1; -; Genomic_DNA.
DR   RefSeq; XP_009569887.1; XM_009571592.1.
DR   AlphaFoldDB; A0A091FFQ8; -.
DR   STRING; 55661.A0A091FFQ8; -.
DR   GeneID; 104068681; -.
DR   KEGG; cuca:104068681; -.
DR   CTD; 9354; -.
DR   OrthoDB; 1554at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
DR   CDD; cd16657; RING-Ubox_UBE4A; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13931:SF16; UBIQUITIN CONJUGATION FACTOR E4 A; 1.
DR   PANTHER; PTHR13931; UBIQUITINATION FACTOR E4; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760}.
FT   DOMAIN          992..1066
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          40..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1075 AA;  123315 MW;  E684977EFCBA99F5 CRC64;
     MTDQENNNSI SSNPFAALFG SIADAKHFAA VQKQQQLRQL RGDEASVSQD DSDNSISESL
     DDCDYSVAEI NRSFRSQREL CEQLNINHMI QRIFLITLDN SDPSMKSGNG IPVRCVYLEE
     MAADLDEQDW LDMDNVEQAL FTRLLLPEPA NHLIYMTSAS TQNLSADRDA GERQILRYLY
     ACFQRAREEI TKVPESLLPF AVRCRNLTVS NTRTVLLTPE IYVNQNVHEQ LVDLMLEALQ
     GAHFEGVTAF LEEVIEALTM DEEVRTFGEV MVPVFDILSG RIKDLDLCQI LLYTYLDVLL
     YFTKQKDIAK VFAGYIQPKD PSNGQMYQKT LLGAILNISC LLKTPGVVEN HGYFLNPSRS
     SPQEIKVQES NIHQFMGQFH EKIYQMLKNL LQLSPETKHR ILSWLGNCLY ANAGRTKIWA
     NQMPEIFFQM YASDAFFLNL GAALLKLCQP FCKPKSPRLL TFNPTYCALK ELNEEERRSK
     NVHMKGLEKE TCLIPAPSEQ EPEFANSYNL VTENLVLTQY TLHLGFHRLH DQMVKINQSL
     HRLQVAWREA QQSASPAADS LREQFERLMT IYLSTKTAMT EPQMLQNCLN LQVSMAVLLV
     QLAMGNHGTE PLELSFPLPE VENSALAYVP EFFADNLGDF FIFLRRFADD ILETSADSLE
     HVLHFITVFM GDVERMKNPH LRAKLAEVLE AVMPHLDQAQ SPLVSSVFHR KRVFCSYRNA
     AHLAEALIKV FVDIEFTGDP HQFEQKFNYR RPMYPILRYM WGTDSYRQSI KALADYASEN
     LEAMNPPLFL RFLNLLMNDA IFLLDEAIQY LSKIKVQQIE KDRGEWDSLS QEARREKESS
     LQMFGQLARF HNIMSNETIG TLAFLTSEIK SLFVHPFLAE RIISMLNYFL QHLVGPKMGA
     LKVKDFSEFD FKPQQLVSDI CTIYLNLGDE ENFCATVPKD GRSYSPTLFA QTVRVLKKIN
     KPGNMIVSFS NLAERIKSLA DRQQQEEETY ADACDEFLDP IMSTLMLDPV ILPSSRVTVD
     RSTIARHLLS DQTDPFNRSP LTMDQIRPNT ELKEKIQQWL AERKKQKEEL EETLN
//